ID A0A0D3VF65_9BACL Unreviewed; 610 AA.
AC A0A0D3VF65;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN ORFNames=UB51_19245 {ECO:0000313|EMBL:AJS60236.1};
OS Paenibacillus sp. IHBB 10380.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS60236.1, ECO:0000313|Proteomes:UP000032320};
RN [1] {ECO:0000313|EMBL:AJS60236.1, ECO:0000313|Proteomes:UP000032320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS60236.1,
RC ECO:0000313|Proteomes:UP000032320};
RX PubMed=25908145;
RA Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using
RT PacBio Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001031, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
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DR EMBL; CP010976; AJS60236.1; -; Genomic_DNA.
DR RefSeq; WP_044878678.1; NZ_CP010976.1.
DR AlphaFoldDB; A0A0D3VF65; -.
DR STRING; 1566358.UB51_19245; -.
DR KEGG; pih:UB51_19245; -.
DR PATRIC; fig|1566358.3.peg.4235; -.
DR HOGENOM; CLU_012520_5_2_9; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000032320; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005855; GFAT.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000032320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 286..425
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 458..600
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 605
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 610 AA; 66683 MW; B6BFA357165E08F9 CRC64;
MCGIVGYIGT QKTQSVLIEG LKKLEYRGYD SAGIAVFTKE GLQVVKAQGR LANLEFKLEE
GPLVGTAGIG HTRWATHGKP SDANSHPHTD ESLKFSVVHN GIIENYLDLK DELMAEGHTF
ASETDTEVIA HLISREYDGD IVKAVQKAIT FMRGAFALGV LTEYEPDRLV AVRQASPLII
GIGEGENFIG SDIPAILQYT RNVYILNDGE MAVLTQDAVE LMTIEGNFIS REMIHVDWDA
VTAEKGGFEH FMLKEIHEQP KAYRDTMRGR IDSEGKNVVF PELKLTREQI MNIRNIQIIA
CGTAYHAGLV GRYVIEQLVR IPVETDVASE YRYRAPIVTP ETLVIVVSQS GETADTLAAL
REAKANGAHV LAITNVVGSS IARDADDVIV TLAGPEIAVA STKAYTSQLI AFYLFGLFLA
EVRGTQTPEA IAHIIAAMQA LPEQLDSMLE HSESIKAYAE QISHHEHLFF IGRGIDFAVV
QEGSLKLKEI SYIHSEAYPA GELKHGTLAL IEDGIPVIAL VTQESVLEKT VSNIKEVSAR
GADIMAFTFE EHVPTLLKSV DQAFAIPKTL PLLTPALSVV PLQLLAYYAS LARGNDVDKP
RNLAKSVTVE
//
